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Cited by 65

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Stoicheiometry and kinetics of the prolyl 4-hydroxylase partial reaction

Jong, Luitzen de, Kemp, Albertus·1984·Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
DOI 10.1016/0167-4838(84)90113-4
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Abstract

In the absence of a peptidylproline substrate, the oxidative decarboxylation of 2-oxoglutarate by prolyl 4-hydroxylase (prolyl-glycyl-peptide,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating), EC 1.14.11.2) is stoicheiometrically coupled to the oxidation of ascorbate. The Km and Kd for O2 in this partial reaction are 1.5 mM, this value being one order of magnitude higher than the Km and Kd for O2 in the complete reaction in the presence of (Pro-Pro-Gly)5, indicating that in this case O2 can become enzyme-bound predominantly after the interaction of the peptide substrate with the enzyme. The Km values for 2-oxoglutarate in the partial and the complete reactions are the same. In the absence of both a peptide substrate and ascorbate 2 mol CO2 per mol enzyme are produced in the first 1-1.5 min, during which the enzyme becomes inactivated and, as shown earlier (De Jong , L., Albracht , S.P.J. and Kemp, A. (1982) Biochim. Biophys. Acta 704, 326-332) enzyme-bound Fe2+ becomes oxidized to Fe3+. The results are consistent with a mechanism in which a Fe2+O complex is the O-transferring intermediate involved in peptidylproline hydroxylation.

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Citations

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Research works printed but not linked: 20

  1. Kivirikko, 1980, Vol. 1, 53
  2. De Jong, 1982, Biochim. Biophys. Acta, 709, 142, 10.1016/0167-4838(82)90431-9 · DOI
  3. De Jong, 1982, Biochim. Biophys. Acta, 704, 326, 10.1016/0167-4838(82)90162-5 · DOI · Paper page
  4. Tuderman, 1977, Eur. J. Biochem., 80, 341, 10.1111/j.1432-1033.1977.tb11888.x · DOI
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  6. Counts, 1978, 75, 2145
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  11. Tuderman, 1975, Eur. J. Biochem., 52, 9, 10.1111/j.1432-1033.1975.tb03967.x · DOI
  12. Hansen, 1969, Biochim. Biophys. Acta, 81, 214
  13. Jagota, 1982, Anal. Biochem., 127, 178, 10.1016/0003-2697(82)90162-2 · DOI
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  20. Warn-Cramer, 1983, J. Biol. Chem., 258, 10551, 10.1016/S0021-9258(17)44491-7 · DOI

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Metadata

Authors
Jong, L. D., & Kemp, A.
Venue
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Publisher
Elsevier BV
Published
1984-05
Volume
787
Issue
1
Pages
105-111
ISSN
0167-4838
DOI
10.1016/0167-4838(84)90113-4
Cited by
65
References
1
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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CoChat. (2026). Citation check: Stoicheiometry and kinetics of the prolyl 4-hydroxylase partial reaction. https://app.cochat.ai/papers/10.1016/0167-4838(84)90113-4
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Jong, L. D., & Kemp, A. (1984). Stoicheiometry and kinetics of the prolyl 4-hydroxylase partial reaction. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. https://doi.org/10.1016/0167-4838(84)90113-4

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.